Helical structures of homo-chiral isotope-labeled α-aminoisobutyric acid peptides

Length-Dependent Formation of Transmembrane Pores by 310-Helical α-Aminoisobutyric Acid Foldamers

The synthetic biology toolbox lacks extendable and conformationally controllable yet easy-to-synthesize building blocks that are long enough to span membranes. To meet this need, an iterative synthesis of α-aminoisobutyric acid (Aib) oligomers was used to create a library of homologous rigid-rod 310-helical foldamers, which have incrementally increasing lengths and functionalizable N- and C-ter...

Application of α-aminoisobutyric acid and β-aminoisobutyric acid inhibits pericarp browning of harvested longan fruit

BACKGROUND Pericarp browning is a critical problem resulting in reduced commercial value and shelf life of longan fruit. RESULTS Two non-protein amino acids, α-aminoisobutyric acid (AIB) and β-aminoisobutyric acid (BAIB) at 100 and 1 mM were applied to longan fruit prior to storage for up to 8 days at 25 °C respectively. Contents of the major five phenolics (gallic acid, catechin, corilagin, ...

Effect of disulphide bond position on salt resistance and LPS-neutralizing activity of α-helical homo-dimeric model antimicrobial peptides.

To investigate the effects of disulphide bond position on the salt resistance and lipopolysaccharide (LPS)-neutralizing activity of α-helical homo-dimeric antimicrobial peptides (AMPs), we synthesized an α-helical model peptide (K6L4W1) and its homo-dimeric peptides (di-K(6)L(4)W(1)-N, di-K(6)L(4)W(1)-M, and di-K(6)L(4)W(1)-C) with a disulphide bond at the N-terminus, the central position, and ...

Normalization Standard Consisting of 1,000 Stable Isotope Labeled Peptides

2D-IR Study of a Photoswitchable Isotope-Labeled α-Helix